Membrane-associated guanylate kinases (MAGUKs) are a family of molecular scaffolds that organize and cluster protein complexes at subcellular specializations. CASK, a multimodular MAGUK containing CamK, PDZ, SH3 and GK domains, is involved in a variety of molecular events including EGF receptor localization and signalling, KIF-17 dependent NMDA receptor containing vesicle transport, presynaptic vesicle exocytosis and basolateral localization of certain transmembrane proteins. CASK also translocates to the nucleus upon interaction with the Tbr-1 transcription factor where it functions as a transcription regulator. We used the CASK PDZ domain in a yeast two-hybrid screen to identify novel members involved in CASK function. TRIP, a TGF-beta Receptor II (TBRII) Interacting Protein that modulates TBRII-dependent gene expression, was identified as a CASK binding protein through its consensus C-terminal PDZ type-II interacting motif. Here we show that CASK, TRIP and TBRII interact in vitro assays, heterologous expression systems and form a tripartite complex in brain.
Identifer | oai:union.ndltd.org:LACETR/oai:collectionscanada.gc.ca:QMM.78377 |
Date | January 2002 |
Creators | Ho, Joanne Wing Yee, 1977- |
Contributors | Shrier, Alvin (advisor) |
Publisher | McGill University |
Source Sets | Library and Archives Canada ETDs Repository / Centre d'archives des thèses électroniques de Bibliothèque et Archives Canada |
Language | English |
Detected Language | English |
Type | Electronic Thesis or Dissertation |
Format | application/pdf |
Coverage | Master of Science (Department of Physiology.) |
Rights | All items in eScholarship@McGill are protected by copyright with all rights reserved unless otherwise indicated. |
Relation | alephsysno: 001974447, proquestno: AAIMQ88212, Theses scanned by UMI/ProQuest. |
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